The behavior of the dielectric properties of gelatin in the frequency range from 10(3) Hz to 10(7) Hz was investigated and compared with that of the globule protein, bovine serum albumin (BSA), desalted gelatin and BSA being used. Dielectric relaxation was observed for both the gelatin and BSA solutions. The relaxation data were fitted well by the Cole-Cole equation; the Cole-Cole parameter (beta) and the relaxation time (tau) were obtained. For the BSA solutions, tau was proportional to the solution viscosity (eta) at 40 degrees C and 25 degrees C, and the values of beta at 40 degrees C were similar to those at 25 degrees C. For gelatin solution, tau was proportional to eta at 40 degrees C, but was not proportional to eta at 25 degrees C. In addition, the values of beta at 25 degrees C were smaller than those at 40 degrees C. These results indicate that the rotation of gelatin and/or polarization of submolecular groups in the coil state greatly contributed to the dielectric relaxation at 40 degrees C; on the other hand, the formation of cross-linking junctions consisting of helix structures would have affected the dielectric relaxation at 25 degrees C.